AnxA7

Annexin A7 (ANXA7) is a calcium- and phospholipid-binding member of the annexin family that participates in membrane fusion, vesicle dynamics, and cellular membrane remodeling processes^[1][2]. Mechanistically, ANXA7 is recruited to damaged cellular membranes in response to calcium influx, where it interacts with apoptosis-linked gene 2 (ALG-2) and ALG-2-interacting protein X (ALIX) to promote assembly of the endosomal sorting complex required for transport III (ESCRT-III) repair machinery^[1]. Through this pathway, ANXA7 enables ESCRT-III-mediated shedding of injured plasma membrane regions and supports efficient plasma membrane repair, a process essential for cell survival after membrane damage^[1]. Recent evidence further demonstrates that ANXA7 also contributes to lysosomal membrane repair, but this activity is mechanistically distinct from its plasma membrane repair function because it occurs independently of ESCRT-III recruitment^[2]. In damaged lysosomes, ANXA7 is proposed to facilitate membrane restoration through membrane curvature induction and membrane cross-linking activities, highlighting its multifunctional role in membrane integrity control^[2]. In disease-related models, ANXA7 has been implicated in multiple cancer contexts, including breast cancer, hepatocellular carcinoma, glioblastoma, prostate cancer, and thyroid cancer, indicating that membrane repair and signaling functions of ANXA7 may influence tumor biology and disease progression^[3][4]. Compared with other annexin family members, ANXA7 contains an unusually long hydrophobic N-terminal domain that contributes to functional specificity and interactions with regulatory proteins, supporting distinct biological activities among annexin isoforms^[1]. These membrane repair mechanisms make ANXA7 a useful experimental target for studies investigating cellular stress responses, membrane damage, cancer biology, and ESCRT-dependent repair pathways^[1][2].

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